node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
clpB | clpP | ECIAI1_2715 | ECIAI1_0441 | Protein disaggregation chaperone; Function experimentally demonstrated in the studied species; factor. | Proteolytic subunit of ClpA-ClpP and ClpX-ClpP ATP-dependent serine proteases; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | 0.972 |
clpB | dnaJ | ECIAI1_2715 | ECIAI1_0015 | Protein disaggregation chaperone; Function experimentally demonstrated in the studied species; factor. | Chaperone Hsp40, co-chaperone with DnaK; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interaction [...] | 0.968 |
clpB | dnaK | ECIAI1_2715 | ECIAI1_0014 | Protein disaggregation chaperone; Function experimentally demonstrated in the studied species; factor. | Chaperone Hsp70, co-chaperone with DnaJ; Function experimentally demonstrated in the studied species; factor. | 0.999 |
clpB | groL | ECIAI1_2715 | ECIAI1_4376 | Protein disaggregation chaperone; Function experimentally demonstrated in the studied species; factor. | Cpn60 chaperonin GroEL, large subunit of GroESL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.963 |
clpB | groS | ECIAI1_2715 | ECIAI1_4375 | Protein disaggregation chaperone; Function experimentally demonstrated in the studied species; factor. | Cpn10 chaperonin GroES, small subunit of GroESL; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.925 |
clpB | grpE | ECIAI1_2715 | ECIAI1_2735 | Protein disaggregation chaperone; Function experimentally demonstrated in the studied species; factor. | Heat shock protein; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-depen [...] | 0.975 |
clpB | hslU | ECIAI1_2715 | ECIAI1_4136 | Protein disaggregation chaperone; Function experimentally demonstrated in the studied species; factor. | Molecular chaperone and ATPase component of HslUV protease; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | 0.957 |
clpB | hslV | ECIAI1_2715 | ECIAI1_4137 | Protein disaggregation chaperone; Function experimentally demonstrated in the studied species; factor. | Peptidase component of the HslUV protease; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. Belongs to the peptidase T1B family. HslV subfamily. | 0.913 |
clpB | htpG | ECIAI1_2715 | ECIAI1_0476 | Protein disaggregation chaperone; Function experimentally demonstrated in the studied species; factor. | Molecular chaperone HSP90 family; Molecular chaperone. Has ATPase activity. | 0.980 |
clpB | tig | ECIAI1_2715 | ECIAI1_0440 | Protein disaggregation chaperone; Function experimentally demonstrated in the studied species; factor. | Peptidyl-prolyl cis/trans isomerase (trigger factor); Function experimentally demonstrated in the studied species; enzyme. | 0.635 |
clpP | clpB | ECIAI1_0441 | ECIAI1_2715 | Proteolytic subunit of ClpA-ClpP and ClpX-ClpP ATP-dependent serine proteases; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | Protein disaggregation chaperone; Function experimentally demonstrated in the studied species; factor. | 0.972 |
clpP | dnaJ | ECIAI1_0441 | ECIAI1_0015 | Proteolytic subunit of ClpA-ClpP and ClpX-ClpP ATP-dependent serine proteases; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | Chaperone Hsp40, co-chaperone with DnaK; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interaction [...] | 0.755 |
clpP | dnaK | ECIAI1_0441 | ECIAI1_0014 | Proteolytic subunit of ClpA-ClpP and ClpX-ClpP ATP-dependent serine proteases; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | Chaperone Hsp70, co-chaperone with DnaJ; Function experimentally demonstrated in the studied species; factor. | 0.902 |
clpP | groL | ECIAI1_0441 | ECIAI1_4376 | Proteolytic subunit of ClpA-ClpP and ClpX-ClpP ATP-dependent serine proteases; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | Cpn60 chaperonin GroEL, large subunit of GroESL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.942 |
clpP | groS | ECIAI1_0441 | ECIAI1_4375 | Proteolytic subunit of ClpA-ClpP and ClpX-ClpP ATP-dependent serine proteases; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | Cpn10 chaperonin GroES, small subunit of GroESL; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.912 |
clpP | grpE | ECIAI1_0441 | ECIAI1_2735 | Proteolytic subunit of ClpA-ClpP and ClpX-ClpP ATP-dependent serine proteases; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | Heat shock protein; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-depen [...] | 0.836 |
clpP | hslU | ECIAI1_0441 | ECIAI1_4136 | Proteolytic subunit of ClpA-ClpP and ClpX-ClpP ATP-dependent serine proteases; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | Molecular chaperone and ATPase component of HslUV protease; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | 0.956 |
clpP | hslV | ECIAI1_0441 | ECIAI1_4137 | Proteolytic subunit of ClpA-ClpP and ClpX-ClpP ATP-dependent serine proteases; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | Peptidase component of the HslUV protease; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. Belongs to the peptidase T1B family. HslV subfamily. | 0.936 |
clpP | htpG | ECIAI1_0441 | ECIAI1_0476 | Proteolytic subunit of ClpA-ClpP and ClpX-ClpP ATP-dependent serine proteases; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | Molecular chaperone HSP90 family; Molecular chaperone. Has ATPase activity. | 0.445 |
clpP | tig | ECIAI1_0441 | ECIAI1_0440 | Proteolytic subunit of ClpA-ClpP and ClpX-ClpP ATP-dependent serine proteases; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | Peptidyl-prolyl cis/trans isomerase (trigger factor); Function experimentally demonstrated in the studied species; enzyme. | 0.656 |